Publication:
C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization

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Issued Date

2017

Resource Type

Article

File Type

application/pdf

ISSN

1681702

DOI

10.1016/j.virusres.2016.09.017

Other identifier(s)

2-s2.0-84992166449

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Virus Research. Vol 227, (2017), p.41-48

Suggested Citation

Somrit M., Watthammawut A., Chotwiwatthanakun C., Ounjai P., Suntimanawong W., Weerachatyanukul W. C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization. Virus Research. Vol 227, (2017), p.41-48. doi:10.1016/j.virusres.2016.09.017 Retrieved from: https://hdl.handle.net/20.500.14740/4280

Title

C-terminal domain on the outer surface of the Macrobrachium rosenbergii nodavirus capsid is required for Sf9 cell binding and internalization

Author(s)

Somrit M.
 Watthammawut A.
 Chotwiwatthanakun C.
 Ounjai P.
 Suntimanawong W.
 Weerachatyanukul W.

Abstract

We have shown that Macrobrachium rosenbergii nodavirus (MrNV) was able to infect Sf9 cells and that MrNV virus-like particles (MrNV-VLPs) were capable nanocontainers for delivering nucleic acid-based materials. Here, we demonstrated that chymotryptic removal of a C-terminal peptide and its truncated variant (F344-MrNV-VLPs) exhibited a drastically reduced ability to interact and internalize into Sf9 cells. Electron microscopic observations revealed that the loss of C-terminal domain either from enzyme hydrolysis or genetic truncation did not affect the generated MrNV-VLPs’ icosahedral conformation, but did drastically affect the VLPs’ internalization ability into Sf9 cells. Homology-based modelling of the MrNV capsid with other icosahedral capsid models revealed that this chymotrypsin-sensitive C-terminal domain was not only exposed on the capsid surface, but also constituted the core of the viral capsid protrusion. These results therefore suggest the importance of the C-terminal domain as a structure for targeted cell interaction which is presumably localized at the protruding domain. This work thus provided the functional insights into the role of the MrNV C-terminal domain in viral entry into Sf9 cells and lead to the development of strategies in combatting MrNV infection in susceptible cells. © 2016 Elsevier B.V.

Subject(s)

Chymotrypsin
 Article
 Carboxy terminal sequence
 Cell interaction
 Controlled study
 Flow cytometry
 Insect cell culture
 Macrobrachium rosenbergii
 Nodaviridae
 Nonhuman
 Priority journal
 Protein hydrolysis
 SF9 cell line
 Shrimp
 Virus attachment
 Virus capsid
 Virus entry
 Virus like agent
 Amino acid sequence
 Animal
 Chemistry
 Host pathogen interaction
 Metabolism
 Molecular model
 Nodaviridae
 Palaemonidae
 Physiology
 Protein conformation
 Protein domain
 Sf9 cell line
 Ultrastructure
 Virology
 Virus assembly
 Virus capsid
 Amino Acid Sequence
 Animals
 Capsid
 Flow Cytometry
 Host-Pathogen Interactions
 Models, Molecular
 Nodaviridae
 Palaemonidae
 Protein Conformation
 Protein Interaction Domains and Motifs
 Sf9 Cells
 Virus Assembly
 Virus Attachment
 Virus Internalization

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URI

https://hdl.handle.net/20.500.14740/4280

Collections

Scopus: Year 1983-2021

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